The goal of the proposed research is to accumulate knowledge on lenticular hydrolytic enzymes wth an ultimate objective of assessing their role in the biochemistry of the lens. Knowledge has formulated in recent years concerning the proteolytic activity in mammalian lens tissue. A number of specific chemical activities have been localized in crude homogenates to purified lens extracts. This presently incomplete knowledge pertains largely to a few proteinases in normal lens tissue, and little is known concerning senile dependent changes in the kinetics or the localization of enzymes within the different regions or organelles in the lens. Although direct biochemical measurements have been employed to advantage to determine quantitative changes in specific metabolic reactions with proteinases, the literature remains confused and incomplete. By isolating organelles, purification, physiochemical and kinetic properties of enzymes offer promise of providing additional and perhaps broader insight into the senile cataract process. The present proposal contemplates an inquiry into the isolation, identification, purification, chemical characteristics and variability of the hydrolytic enzymes in cellular organelle and different regions of both normal and senile cataractous human lenses. The rapid loss of protein associated with senile cataractogenesis may indicate such a possibility. The study outline in this proposal is designed to examine this hypothesis and accumulate information which may aid in establishing a better understanding of the function of hydrolytic enzymes in lenticular tissue.